(data stored in ACNUC7421 zone)

SWISSPROT: UBIG_METNO

ID   UBIG_METNO              Reviewed;         249 AA.
AC   B8IUB0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000255|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.222 {ECO:0000255|HAMAP-Rule:MF_00472};
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_00472};
GN   Name=ubiG {ECO:0000255|HAMAP-Rule:MF_00472};
GN   OrderedLocusNames=Mnod_0108;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation
CC       steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_00472}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3-
CC       demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n.
CC       {ECO:0000255|HAMAP-Rule:MF_00472}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3-(all-trans-
CC       polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-
CC       methoxy-6-(all-trans-polyprenyl)phenol. {ECO:0000255|HAMAP-
CC       Rule:MF_00472}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00472}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_00472}.
DR   EMBL; CP001349; ACL55155.1; -; Genomic_DNA.
DR   RefSeq; WP_012634394.1; NC_011894.1.
DR   ProteinModelPortal; B8IUB0; -.
DR   SMR; B8IUB0; -.
DR   STRING; 460265.Mnod_0108; -.
DR   EnsemblBacteria; ACL55155; ACL55155; Mnod_0108.
DR   KEGG; mno:Mnod_0108; -.
DR   eggNOG; ENOG4107RFD; Bacteria.
DR   eggNOG; COG2227; LUCA.
DR   HOGENOM; HOG000278064; -.
DR   KO; K00568; -.
DR   OMA; GTHDWEK; -.
DR   OrthoDB; POG091H064Z; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01983; UbiG; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8IUB0.
DR   SWISS-2DPAGE; B8IUB0.
KW   Complete proteome; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT   CHAIN         1    249       Ubiquinone biosynthesis O-
FT                                methyltransferase.
FT                                /FTId=PRO_1000135507.
FT   BINDING      41     41       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING      72     72       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
FT   BINDING      93     93       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00472}.
FT   BINDING     136    136       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00472}.
SQ   SEQUENCE   249 AA;  26956 MW;  90EB5BB1310A3C65 CRC64;
     MSETTGPSID RDEVARFERI AATWWDEAGP MRVLHRFNPV RITYIRDTVC RHFGRDPRRP
     LPLEALSLID IGCGGGILSE PLARLGATVT GLDPAPTNIR VAQAHAAEAG VPVDYRGQTI
     EAVVEAGERF DVVLAMEVVE HVVDMPAFVR TACAAVKPGG LFFAATLNRT MRSFALAIVG
     AEYVLGWLPR GTHDWEKFVT PAELTGAVES AGLTVIDTTG VVYNPLGGRW AMSRDTGVNY
     MIAAERPVA
//

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